Superoxide Dismutase family

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Last update: 2021-12-02 (Bruno Savelli)

Superoxide Dismutase family: FeSOD, MnSOD and Cu/ZnSOD, SOD like and Copper chaperone for SOD


Superoxide dismutase (SOD, EC is an enzyme that alternately catalyzes the dismutation (or partitioning) of the superoxide (O2.-) radical into either ordinary molecular oxygen (O2) or hydrogen peroxide (H2O2). Superoxide is produced as a by-product of oxygen metabolism and, if not regulated, causes many types of cell damage.
SOD catalyzed dismutation of superoxide with the following half-reactions applicable to all the different metal-coordinated forms of SOD:

M(n+1)+-SOD + O2.- Mn+-SOD + O2
Mn+-SOD + O2.- + 2H+ M(n+1)+-SOD + H2O2

where M = Cu (n=1) ; Mn (n=2) ; Fe (n=2) ; Ni (n=2).,Zn

In all mammals, and most chordates 3 SOD have been detected: two copper and zinc SOD (SOD1 located in the cytoplasm, SOD2 in the mitochondria), and one MnSOD (SOD3 extracellular).
In plants, there are three SOD classes. FeSOD (homodimer and tetramer found in chlorplast), MnSOD (homodimer and homotetramer mainly found in mitochondrion and peroxisomes) and CuZnSOD (in the chloroplast and cytosol).
In prokaryote, iron or manganes SOD can be found together with Nickel-containing SOD.


Iron and manganese superoxide dismutases (FeSOD and MnSOD) :
Pfam: PF02777
Iron/manganese superoxide dismutases
C-terminal domain and PF00081
Iron/manganese superoxide dismutases
alpha-hairpin domain
Interpro: IPR019832
Manganese/iron superoxide dismutase
C-terminal and IPR001189
Manganese/iron superoxide dismutase
alpha-hairpin domain.

Copper/zinc superoxide dismutase (SODC)
Pfam: PF00080
Interpro: IPR001424
Superoxide dismutase
copper/zinc binding domain.

Nickel superoxide dismutase (NiSOD)
Pfam: PF09055
Nickel-containing superoxide dismutase
Interpro: IPR014123
Nickel-containing superoxide dismutase.


Robinett NG, Peterson RL, Culotta VC. Eukaryotic copper-only superoxide dismutases (SODs): A new class of SOD enzymes and SOD-like protein domains. J Biol Chem. 2018 Mar 30;293(13):4636-4643. PMID 29259135